Is AlphaFold just making a good estimate of the protein structure?
AlphaFold (version 1 and 2) predicts (so estimates) the 3D shape of the protein from the sequence of amino acids. AlphaFold's performance is measured with the global distance test (GDT), which is a measure of similarity between two protein structures (the prediction and the ground-truth) that ranges from 0 to 100.
There is a short video and a longer one (both by DeepMind) that summarise the issue of protein folding, how it is important, how well AlphaFold approximately solves it (in the competition Critical Assessment of protein Structure Prediction (CASP)), i.e. AlphaFold 2 achieves a median GDT score of 92.4 (and 87 on the hardest proteins), which is a lot higher than AlphaFold 1's GDT score of 58 (which was the highest achieved score at the time), where, according to John Moult (president of CASP), a score around 90 is considered a satisfactory solution to the protein folding problem. You can find more details about AlphaFold 2 in this DeepMind blog post and about AlphaFold 1 in this other blog post or the associated paper published in Nature this year. You can find the code for AlphaFold 1 here, but there are other community/open-source implementations.
Despite the importance of the problem and achievement, there is clearly a lot of hype about this breakthrough (given also that it was achieved by DeepMind). This is also discussed in this video by Lex Fridman.